RNA-binding residues prediction using structural features

被引:22
|
作者
Ren, Huizhu [1 ,2 ]
Shen, Ying [3 ,4 ]
机构
[1] Tianjin Med Univ, Minist Hlth, Metab Dis Hosp, Key Lab Hormones & Dev,Collaborat Innovat Ctr Tia, Tianjin 300070, Peoples R China
[2] Tianjin Med Univ, Tianjin Inst Endocrinol, Tianjin 300070, Peoples R China
[3] Tongji Univ, Sch Software Engn, Shanghai 201804, Peoples R China
[4] Nanjing Univ Sci & Technol, Key Lab Intelligent Percept & Syst High Dimens In, Minist Educ, Nanjing 210094, Jiangsu, Peoples R China
来源
BMC BIOINFORMATICS | 2015年 / 16卷
关键词
Protein-RNA interaction prediction; Structural information; Least-squares distance; AMINO-ACID-SEQUENCE; WEB SERVER; PROTEINS; SITES; DNA; INFORMATION; SURFACES; PROFILE; PLUS;
D O I
10.1186/s12859-015-0691-0
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Background: RNA-protein complexes play an essential role in many biological processes. To explore potential functions of RNA-protein complexes, it's important to identify RNA-binding residues in proteins. Results: In this work, we propose a set of new structural features for RNA-binding residue prediction. A set of template patches are first extracted from RNA-binding interfaces. To construct structural features for a residue, we compare its surrounding patches with each template patch and use the accumulated distances as its structural features. These new features provide sufficient structural information of surrounding surface of a residue and they can be used to measure the structural similarity between the surface surrounding two residues. The new structural features, together with other sequence features, are used to predict RNA-binding residues using ensemble learning technique. Conclusions: The experimental results reveal the effectiveness of the proposed structural features. In addition, the clustering results on template patches exhibit distinct structural patterns of RNA-binding sites, although the sequences of template patches in the same cluster are not conserved. We speculate that RNAs may have structure preferences when binding with proteins.
引用
收藏
页数:10
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